ID   GBG5_RAT                Reviewed;          68 AA.
AC   P63219; P30670; Q61015;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 136.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5;
DE   Flags: Precursor;
GN   Name=Gng5; Synonyms=Gngt5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1549114; DOI=10.1128/mcb.12.4.1585-1591.1992;
RA   Fisher K.J., Aronson N.N. Jr.;
RT   "Characterization of the cDNA and genomic sequence of a G protein gamma
RT   subunit (gamma 5).";
RL   Mol. Cell. Biol. 12:1585-1591(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as a modulator or transducer in various transmembrane signaling
CC       systems. The beta and gamma chains are required for the GTPase
CC       activity, for replacement of GDP by GTP, and for G protein-effector
CC       interaction.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the G protein gamma family. {ECO:0000305}.
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DR   EMBL; M95780; AAA41188.1; -; mRNA.
DR   EMBL; BC058469; AAH58469.1; -; mRNA.
DR   RefSeq; NP_077353.1; NM_024377.1.
DR   RefSeq; XP_017445483.1; XM_017589994.1.
DR   RefSeq; XP_017460456.1; XM_017604967.1.
DR   AlphaFoldDB; P63219; -.
DR   SMR; P63219; -.
DR   STRING; 10116.ENSRNOP00000021358; -.
DR   PhosphoSitePlus; P63219; -.
DR   jPOST; P63219; -.
DR   PaxDb; 10116-ENSRNOP00000021358; -.
DR   Ensembl; ENSRNOT00000105080.1; ENSRNOP00000087679.1; ENSRNOG00000063636.1.
DR   Ensembl; ENSRNOT00055023963; ENSRNOP00055019557; ENSRNOG00055013943.
DR   Ensembl; ENSRNOT00055029160; ENSRNOP00055023458; ENSRNOG00055017204.
DR   Ensembl; ENSRNOT00055040267; ENSRNOP00055032705; ENSRNOG00055023432.
DR   Ensembl; ENSRNOT00060001078; ENSRNOP00060000383; ENSRNOG00060000865.
DR   Ensembl; ENSRNOT00060022638; ENSRNOP00060017950; ENSRNOG00060013287.
DR   Ensembl; ENSRNOT00060051767; ENSRNOP00060043033; ENSRNOG00060029821.
DR   Ensembl; ENSRNOT00065003177; ENSRNOP00065002180; ENSRNOG00065002419.
DR   Ensembl; ENSRNOT00065020970; ENSRNOP00065016175; ENSRNOG00065012832.
DR   Ensembl; ENSRNOT00065058607; ENSRNOP00065048255; ENSRNOG00065034110.
DR   GeneID; 79218; -.
DR   KEGG; rno:108349548; -.
DR   KEGG; rno:79218; -.
DR   AGR; RGD:11485321; -.
DR   AGR; RGD:620807; -.
DR   CTD; 108349548; -.
DR   CTD; 2787; -.
DR   RGD; 620807; Gng5.
DR   VEuPathDB; HostDB:ENSRNOG00000038205; -.
DR   eggNOG; KOG4119; Eukaryota.
DR   GeneTree; ENSGT01100000263525; -.
DR   HOGENOM; CLU_168377_3_0_1; -.
DR   InParanoid; P63219; -.
DR   OrthoDB; 2872810at2759; -.
DR   PhylomeDB; P63219; -.
DR   TreeFam; TF319909; -.
DR   Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-RNO-202040; G-protein activation.
DR   Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-RNO-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-RNO-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-RNO-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-RNO-4086398; Ca2+ pathway.
DR   Reactome; R-RNO-416476; G alpha (q) signalling events.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-418597; G alpha (z) signalling events.
DR   Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR   Reactome; R-RNO-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-RNO-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   PRO; PR:P63219; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000015936; Expressed in quadriceps femoris and 19 other cell types or tissues.
DR   GO; GO:0031680; C:G-protein beta/gamma-subunit complex; IDA:MGI.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0031681; F:G-protein beta-subunit binding; IBA:GO_Central.
DR   GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:RGD.
DR   GO; GO:0072513; P:positive regulation of secondary heart field cardioblast proliferation; ISO:RGD.
DR   CDD; cd00068; GGL; 1.
DR   Gene3D; 4.10.260.10; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   InterPro; IPR015898; G-protein_gamma-like_dom.
DR   InterPro; IPR036284; GGL_sf.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   PANTHER; PTHR13809:SF5; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(O) SUBUNIT GAMMA-5-RELATED; 1.
DR   PANTHER; PTHR13809; GUANINE NUCLEOTIDE-BINDING PROTEIN GAMMA SUBUNIT; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM01224; G_gamma; 1.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
DR   Genevisible; P63219; RN.
PE   3: Inferred from homology;
KW   Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW   Phosphoprotein; Prenylation; Reference proteome; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P63218"
FT   CHAIN           2..65
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(O)
FT                   subunit gamma-5"
FT                   /id="PRO_0000012631"
FT   PROPEP          66..68
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012632"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P63218"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P63218"
FT   MOD_RES         65
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           65
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   68 AA;  7318 MW;  9AF7A16558863602 CRC64;
     MSGSSSVAAM KKVVQQLRLE AGLNRVKVSQ AAADLKQFCL QNAQHDPLLT GVSSSTNPFR
     PQKVCSFL
//